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Magnesium in PDB 2r92: Elongation Complex of Rna Polymerase II with Artificial Rdrp Scaffold
Enzymatic activity of Elongation Complex of Rna Polymerase II with Artificial Rdrp Scaffold
All present enzymatic activity of Elongation Complex of Rna Polymerase II with Artificial Rdrp Scaffold:
2.7.7.6;
2.7.7.6;
Protein crystallography data
The structure of Elongation Complex of Rna Polymerase II with Artificial Rdrp Scaffold, PDB code: 2r92
was solved by
E.Lehmann,
F.Brueckner,
P.Cramer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 50.00 / 3.80 |
| Space group | C 2 2 21 |
| Cell size a, b, c (Å), α, β, γ (°) | 222.675, 393.853, 283.551, 90.00, 90.00, 90.00 |
| R / Rfree (%) | 21.2 / 24.6 |
Other elements in 2r92:
The structure of Elongation Complex of Rna Polymerase II with Artificial Rdrp Scaffold also contains other interesting chemical elements:
| Zinc | (Zn) | 8 atoms |
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Elongation Complex of Rna Polymerase II with Artificial Rdrp Scaffold
(pdb code 2r92). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Elongation Complex of Rna Polymerase II with Artificial Rdrp Scaffold, PDB code: 2r92:
In total only one binding site of Magnesium was determined in the Elongation Complex of Rna Polymerase II with Artificial Rdrp Scaffold, PDB code: 2r92:
Magnesium binding site 1 out of 1 in 2r92
Go back to
Magnesium Binding Sites List in 2r92
Magnesium binding site 1 out
of 1 in the Elongation Complex of Rna Polymerase II with Artificial Rdrp Scaffold
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Elongation Complex of Rna Polymerase II with Artificial Rdrp Scaffold within 5.0Å range:
|
Reference:
E.Lehmann,
F.Brueckner,
P.Cramer.
Molecular Basis of Rna-Dependent Rna Polymerase II Activity. Nature V. 450 445 2007.
ISSN: ISSN 0028-0836
PubMed: 18004386
DOI: 10.1038/NATURE06290
Page generated: Wed Aug 14 03:19:01 2024
ISSN: ISSN 0028-0836
PubMed: 18004386
DOI: 10.1038/NATURE06290
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